+Open data
-Basic information
Entry | Database: PDB / ID: 6a1s | ||||||
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Title | Charcot-Leyden crystal protein/Galectin-10 variant E33A | ||||||
Components | Galectin-10 | ||||||
Keywords | PROTEIN BINDING / Charcot-Leyden crystal protein/Galectin-10 | ||||||
Function / homology | Function and homology information regulation of activated T cell proliferation / regulation of T cell cytokine production / T cell apoptotic process / regulation of T cell anergy / cysteine-type endopeptidase activity involved in apoptotic process / carbohydrate binding / collagen-containing extracellular matrix / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.63 Å | ||||||
Authors | Su, J. | ||||||
Funding support | China, 1items
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Citation | Journal: Glycobiology / Year: 2019 Title: Identification of key amino acid residues determining ligand binding specificity, homodimerization and cellular distribution of human galectin-10 Authors: Su, J. / Song, C. / Si, Y. / Cui, L. / Yang, T. / Li, Y. / Wang, H. / Tai, G. / Zhou, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6a1s.cif.gz | 47.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6a1s.ent.gz | 32.5 KB | Display | PDB format |
PDBx/mmJSON format | 6a1s.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6a1s_validation.pdf.gz | 424.2 KB | Display | wwPDB validaton report |
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Full document | 6a1s_full_validation.pdf.gz | 424.9 KB | Display | |
Data in XML | 6a1s_validation.xml.gz | 10 KB | Display | |
Data in CIF | 6a1s_validation.cif.gz | 14.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a1/6a1s ftp://data.pdbj.org/pub/pdb/validation_reports/a1/6a1s | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 16696.072 Da / Num. of mol.: 1 / Fragment: UNP residues 1-142 / Mutation: E33A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CLC / Production host: Escherichia coli (E. coli) / References: UniProt: Q05315 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.78 Å3/Da / Density % sol: 55.68 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / Details: Bistris |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL18U1 / Wavelength: 0.98 Å |
Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: Nov 11, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 1.63→19.64 Å / Num. obs: 24150 / % possible obs: 99.6 % / Redundancy: 18.8 % / Net I/σ(I): 20.5 |
Reflection shell | Resolution: 1.63→1.66 Å |
-Processing
Software | Name: PHENIX / Version: (1.13_2998: ???) / Classification: refinement | ||||||||||||||||||||||||
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.63→19.637 Å / SU ML: 0.12 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 16.87 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||
Displacement parameters | Biso max: 54.77 Å2 / Biso mean: 15.1298 Å2 / Biso min: 5.07 Å2 | ||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 1.63→19.637 Å
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